Glycoprotein biosynthesis in splenic cells. Purification of a microsomal galactosyl-transferase

Abstract

One part of the microsomal galactosyl-transferase activity of splenic cells of rats can by solubilized by the action of Triton X-100 and Tween 20. Its purification on a Sephadex G-200 column and by electrophoresis on a polyacrylamide gel leads to a solution of high specific enzymic activity.

Role of galactosyl-transferases in rat gastric epithelial glycoprotein synthesis

“…As shown for liver (Fraser and Mookerjea [19], Schachter et al [20]), mammary gland (Smith and Brew [21]), and spleen cells (Martin et al [22]), Golgi membranes contain a galactosyl-transferase activity towards modified high molecular weight acceptors like fetuin and al-acid glycoprotein as well as towards free GlcNAc. In all cases, the enzyme catalyzes the formation of galactosyl-~(1-4)acetylglucosaminyl linkages.…”